GL1X · GenesisL1 explorer

Research workbench

Crystal structure of S-adenosylmethionine decarboxylase proenzyme (TM0655) from thermotoga maritima at 1.2 a resolution

Analyse Crystal structure of S-adenosylmethionine decarboxylase proenzyme (TM0655) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VR7
Type
protein
Length
238 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
S-adenosylmethionine decarboxylase proenzyme
EC
4.1.1.50
UniProt
Q9WZC3

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine decarboxylase proenzyme (EC 4.1.1.50)protein12032% helix, 45% strandQ9WZC3
BS-adenosylmethionine decarboxylase proenzyme (EC 4.1.1.50)protein11829% helix, 45% strandQ9WZC3

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 1542 Ų buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

  • 1VR7 · Crystal structure of S-adenosylmethionine decarboxylase proenzyme (TM0655) from… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WZC3 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme… · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.